Taylor & Francis Group
Browse
1/1
6 files

Characterization of a novel shell matrix protein with vWA domain from Mytilus coruscus

dataset
posted on 2020-04-21, 15:02 authored by Qi Sun, Yuting Jiang, Meihua Fan, Xiaolin Zhang, Huanzhi Xu, Zhi Liao

Mollusk shell is a product of biomineralization with excellent mechanical properties, and the shell matrix proteins (SMPs) have important functions in shell formation. A vWA domain-containing protein (VDCP) was identified from the shell of Mytilus coruscus as a novel shell matrix protein. The VDCP gene is expressed at a high level in specific locations in the mantle and adductor muscle. Recombinant VDCP (rVDCP) showed abilities to alter the morphology of both calcite and aragonite, induce the polymorph change of calcite, bind calcite, and decrease the crystallization rate of calcite. In addition, immunohistochemistry analyses revealed the specific location of VDCP in the mantle, the adductor muscle, and the myostracum layer of the shell. Furthermore, a pull-down analysis revealed eight protein interaction partners of VDCP in shell matrices and provided a possible protein–protein interaction network of VDCP in the shell.

Sequence characterization, recombinant expression, biomineralization-related function, and localization of a vWA domain-containing protein (VDCP) identified from Mytilus corusus shell.

Funding

This work was supported by the Bureau of Science and Technology of Zhoushan [2019F12004]; National Natural Science Foundation of China [31671009].

History